{"title":"M protein of type 12 Strepto coccus pyogenes. Isolation by electrofocusing and some molecular weight-dependent properties.","authors":"Jircaron;í Havlíček","doi":"10.1159/000162735","DOIUrl":null,"url":null,"abstract":"A method for the isolation and purification of M protein was developed. Purified cell walls were sonically disrupted, solubilized M protein was precipitated by ammonium sulphate and then electrofocused. Both in this material and in hot acid extracts type-specific trypsin-sensitive antigens with two separately precipitating moieties were found. Evidence is adduced showing that they both belong to the M protein complex. The molecular weight of our purified M protein ranged between 400,000 and 20,000 daltons, giving a peak at 150,000 daltons. The pI of this material was found to be 5.4-5.6. There were marked differences between the behaviour of the low, medium and high molecular weight fractions obtained from purified M protein by gel filtration.","PeriodicalId":19854,"journal":{"name":"Pathologia et microbiologia","volume":"58 1","pages":"147-58"},"PeriodicalIF":0.0000,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"8","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Pathologia et microbiologia","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1159/000162735","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 8
Abstract
A method for the isolation and purification of M protein was developed. Purified cell walls were sonically disrupted, solubilized M protein was precipitated by ammonium sulphate and then electrofocused. Both in this material and in hot acid extracts type-specific trypsin-sensitive antigens with two separately precipitating moieties were found. Evidence is adduced showing that they both belong to the M protein complex. The molecular weight of our purified M protein ranged between 400,000 and 20,000 daltons, giving a peak at 150,000 daltons. The pI of this material was found to be 5.4-5.6. There were marked differences between the behaviour of the low, medium and high molecular weight fractions obtained from purified M protein by gel filtration.
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